Multiple proteases secreted by a thermophilic actinomycete Streptomyces megasporus SDP4 after 18 h of growth at 55 °C are reported. The enzyme preparation exhibited activity over a broad pH and temperature range of pH 6-12 and 25-85 °C, respectively. Optimum activity was observed at pH 8.0, pH 10.0 and 55 °C and was calcium independent. Thermostability was enhanced in the presence of 0.01 mol l−1 calcium ions and half-life was 30 min at 85 °C. The enzyme was active in the presence of SDS. Both, EDTA and PMSF were partially inhibitory, indicating the presence of serine and metal requiring proteases. Three active zones in the range of 90-30 kDa were detected post-electrophoretically.